To determine the effects of deer antler velvet on maximal aerobic performance and the trainability of muscular strength and endurance, 38 active males were randomly assigned in a double-blind fashion to either deer antler velvet extract ( n = 12), powder ( n = 13), or placebo groups ( n = 13). Subjects were tested prior to beginning supplementation and a 10-week strength program, and immediately post-training. All subjects were measured for circulating levels of testosterone, insulin-like growth factor, erythropoietin, red cell mass, plasma volume, and total blood volume. Additionally, muscular strength, endurance, and VO 2max were determined. All groups improved 6 RM strength equivalently (41 ± 26%, p < .001), but there was a greater increase in isokinetic knee extensor strength (30 ± 21% vs. 13 ± 15%, p = .04) and endurance (21 ± 19% vs. 7 ± 12%, p = .02) in the powder compared to placebo group. There were no endocrine, red cell mass or VO 2max changes in any group. These findings do not support an erythropoetic or aerobic ergogenic effect of deer antler velvet. Further, the inconsistent findings regarding the effects of deer antler velvet powder supplementation on the development of strength suggests that further work is required to test the robustness of the observation that this supplement enhances the strength training response and to ensure this observation is not a type I error.
Mercury-containing intermediates have been isolated from the reaction of 6-deoxyhex-5-enopyranosyl compounds with mercury(II) salts in aqueous acetone. They react to give 2-deoxyinosose derivatives on further exposure to the conditions of their formation or, after isolation, by treatment with hydrogen sulphide. Mercury(II) acetate is more efficient than the previously used mercury(II) chloride for this carbohydrate-into-deoxyinosose conversion.
$^{a}$ G. Reiser, O. Dopfer R. Lindne***, G. Henri, K. M\{u}ller-Dethlefs, E.W. Schlag, and S.D. Colson, Chem. Phys. Lett. 181, 1 (1991). $^{b}$ E. Beiske, M.W. Rainburn, I.M. Atkinson, and A.E.W. Knight, J. Chem. Phys. 91, 752 (1989).
Exposure to UV in humans resulting in sunburn triggers a complex series of events that are a mix of immediate and delayed damage mediation and healing. While studies on the effects of UV exposure on DNA damage and repair have been reported, changes in the oxidative modification of skin proteins are poorly understood at the molecular level, despite the important role played by structural proteins in skin tissue, and the effect of the integrity of these proteins on skin appearance and health. Proteomic molecular mapping of oxidation was here applied to try to enhance understanding of skin damage and recovery from oxidative damage and UVB exposure.A redox proteomic-based approach was applied to evaluating skin protein modification when exposed to varying doses of UVB after initial oxidative stress, via tracking changes in protein oxidation during the healing process in vitro using a full-thickness reconstituted human skin tissue model. Bioassays and structural evaluation confirmed that our cultured skin tissues underwent a normal physiological response to UVB exposure.A set of potential skin marker peptides was generated, for use in tracking skin protein oxidative modification. Exposure to UVB after thermal oxidative stress was found to result in higher levels of skin protein oxidation than a non-irradiated control for up to seven days after exposure. Recovery of the skin proteins from oxidative stress, as assessed by the overall protein oxidation levels, was found to be impaired by UVB exposure. Oxidative modification was largely observed in skin structural proteins.Exposure of skin proteins to UVB exacerbates oxidative damage to structural skin proteins, with higher exposure levels leading to increasingly impaired recovery from this damage. This has potential implications for the functional performance of the proteins and inter-related skin health and cosmetic appearance.
The use of deer velvet antler (DVA) as a potent traditional medicine ingredient goes back for over 2000 years in Asia. Increasingly, though, DVA is being included as a high protein functional food ingredient in convenient, ready to consume products in Korea and China. As such, it is a potential source of endogenous bioactive peptides and of 'cryptides', i.e. bioactive peptides enzymatically released by endogenous proteases, by processing and/or by gastrointestinal digestion. Fermentation is an example of a processing step known to release bioactive peptides from food proteins. In this study, we aimed to identify in silico bioactive peptides and cryptides in DVA, before and after fermentation, and subsequently to validate the major predicted bioactivity by in vitro analysis.Peptides that were either free or located within proteins were identified in the DVA samples by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by database searching. Bioactive peptides and cryptides were identified in silico by sequence matching against a database of known bioactive peptides. Angiotensin-converting enzyme (ACE) inhibitory activity was measured by a colorimetric method.Three free bioactive peptides (LVVYPW, LVVYPWTQ and VVYPWTQ) were solely found in fermented DVA, the latter two of which are known ACE inhibitors. However matches to multiple ACE inhibitor cryptides were obtained within protein and peptide sequences of both unfermented and fermented DVA. In vitro analysis showed that the ACE inhibitory activity of DVA was more pronounced in the fermented sample, but both unfermented and fermented DVA had similar activity following release of cryptides by simulated gastrointestinal digestion.DVA contains multiple ACE inhibitory peptide sequences that may be released by fermentation or following oral consumption, and which may provide a health benefit through positive effects on the cardiovascular system. The study illustrates the power of in silico combined with in vitro methods for analysis of the effects of processing on bioactive peptides in complex functional ingredients like DVA.
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